Reaction-Path Energetics and Kinetics of the Hydride Transfer Reaction Catalyzed by Dihydrofolate Reductase
Author:
Affiliation:
1. Department of Chemistry and Minnesota Supercomputing Institute, University of Minnesota, Minneapolis, Minnesota 55455
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi034824f
Reference107 articles.
1. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
2. Mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli: pH and deuterium isotope effects with NADPH as the variable substrate
3. Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin
4. Determination by Raman Spectroscopy of the pKa of N5 of Dihydrofolate Bound to Dihydrofolate Reductase: Mechanistic Implications
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